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Cardiac CPT (show DHDDS Proteins)-1b suppression protects against the aggravation of cardiac morphology and function associated with HFD feeding. CPT (show DHDDS Proteins)-1b represents a potential therapeutic target for the treatment of cardiac dysfunction related to metabolic diseases such as obesity and diabetes.
Data show that peroxisome-proliferator-activated receptor beta (show PPARD Proteins)/delta (PPARbeta (show PPARD Proteins)/delta) activation restored the lipid-induced endothelial dysfunction by up-regulation of carnitine palmitoyltransferase)-1 (CPT-1 (show CPT1A Proteins)).
Data (including data from knockout and chimeric mice) suggest that Cpt1b is involved in myocardial function (but perhaps not in skeletal muscle function); knockout (and presumably inhibition) of Cpt1b results in cardiac hypertrophy and early death.
CD8 T cells are involved in skeletal muscle regeneration through facilitating MCP-1 secretion and Gr1(high) macrophage infiltration.
CPT1b deficiency can cause lipotoxicity in the heart under pathological stress, leading to exacerbation of cardiac pathology.
Data show that HIV protease inhibitors suppress fatty acid oxidation in skeletal muscle cells, which may be related to decreases in cytosolic- and mitochondrial-associated fatty acid transporters such as CD36 (show CD36 Proteins) and carnitine palmitoyltransferase I (show CPT1A Proteins) .
Leptin reduces the sensitivity of cardiac CPT-I to malonyl-CoA.
generated angiotensin II from angiotensin I in a time-dependent manner; data suggest that MCP-1 might possess a physiological role in angiotensin II formation
both the accumulation and the longevity of MCP-1 in blood is due to complex formation, protecting it from a pathway that rapidly clears MCP-2, which is unable to form complexes with serpins
a detailed analysis of the extended cleavage specificity of mMCP-1 was performed; high selectivity in the P2, P1, P1' and P2' positions indicate that mMCP-1 has a relatively narrow set of in vivo substrates
CPT1 (show CPT1A Proteins) is active on the outer surface of mitochondria and serves as a regulatory site for fatty acid oxidation due to its sensitivity for malonyl-CoA. CPT1b is the muscle isoform.
In subjects with PTSD, significant over-expression of CPT1B was also observed in the two common dysregulated pathways: fatty acid metabolism and PPAR (show PPARA Proteins).
Differential DNA methylation (show HELLS Proteins) may underlie the depressed expression of CPT1B in response to lipid, contributing to the metabolic inflexibility associated with severe obesity.
E531K substitution in CPT1B decreases the mitochondrial beta-oxidation pathway, which increases the non-protein respiratory quotient value during recovery from exercise.
study identified a novel haplotype consisting of the indel variation, which had not been detected in previous studies in Japanese and Korean populations, and observed four single-nucleotide polymorphisms in CHKB (show CHKB Proteins)/CPT1B
CPT1B heterozygous variants of G320D and S427C among control subjects showed significantly higher levels of total and free carnitine in the blood compared to acute myocardial infarction patients.
present results confirm the association of carnitine palmitoyltransferase 1B coding polymorphisms with the metabolic syndrome
Genetic mutations causative for McArdle disease, carnitine palmitoyl transferase deficiency 2, myoadenylate deaminase (show AMPD1 Proteins) deficiency, and malignant hyperthermia have all been associated with Exertional rhabdomyolysis.
The study extends on the observation of a strong multiethnic association of polymorphisms in the TCRA and P2RY11 with narcolepsy, but does not confirm the association of CPT1B/CHKB (show CHKB Proteins) (rs5770917) in the Chinese population.
Genetic analysis, comparison, and tissue distribution of CPT1b
Suppression of CPT1B and induction of SCD (show SCD Proteins) and CEBPB (show CEBPB Proteins) by supplemental arginine promotes increased adiposity in Angus steers.
This study evaluated the effects of nonesterified fatty acids and glucose on carnitine palmitoyltransferase-I (CPT-I) mRNA expression in cultured bovine hepatocytes using real-time reverse transcription polymerase chain reaction and ELISA methods.
Recombinant pig carnitine palmitoyltransferase I (show CPT1A Proteins) beta has unique kinetic characteristics which make it a useful model to study the structure-function relationship of the CPTI enzymes.
Postnatal increases in CPT I activity during the suckling period are accompanied by increased tissue carnitine.
The protein encoded by this gene, a member of the carnitine/choline acetyltransferase family, is the rate-controlling enzyme of the long-chain fatty acid beta-oxidation pathway in muscle mitochondria. This enzyme is required for the net transport of long-chain fatty acyl-CoAs from the cytoplasm into the mitochondria. Multiple transcript variants encoding different isoforms have been found for this gene, and read-through transcripts are expressed from the upstream locus that include exons from this gene.
carnitine O-palmitoyltransferase 1, muscle isoform
, carnitine O-palmitoyltransferase I, mitochondrial muscle isoform
, carnitine palmitoyltransferase I-like protein
, CPT I
, CPT-Ibeta 1
, CPT-Ibeta 3
, Carnitine palmitoyltransferase 1 beta, muscle isoform
, Carnitine palmitoyltransferase 1, muscle
, carnitine O-palmitoyltransferase I, muscle isoform
, carnitine palmitoyltransferase Ibeta 1
, carnitine palmitoyltransferase Ibeta 2
, carnitine palmitoyltransferase Ibeta 3
, carnitine palmitoyl transferase I muscle isoform
, carnitine palmitoyltransferase I
, carnitine palmitoyltransferase 1B
, carnitine palmitoyltransferase 1A like
, carnitine palmitoyltransferase 1B (muscle)
, carnitine palmitoyltransferase 1B-like
, carnitine O-palmitoyltransferase 1, muscle isoform-like
, muscle-type carnitine palmitoyltransferase I